Literature summary for 7.2.2.9 extracted from

Banci, L.; Bertini, I.; Cantini, F.; Migliardi, M.; Natile, G.; Nushi, F.; Rosato, A.
Solution structures of the actuator domain of ATP7A and ATP7B, the Menkes and Wilson disease proteins (2009), Biochemistry, 48, 7849-7855.

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Protein Variants

Protein Variants	Comment	Organism
G853R	the mutation occurring in the A-domain of ATP7A affects the network of communication with the other domains of the enzyme	Homo sapiens
G860V	the mutation occurring in the A-domain of ATP7A destabilizes the fold of the domain	Homo sapiens
L873R	the mutation occurring in the A-domain of ATP7A affects the network of communication within the domain	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q04656	ATP7A and ATP7B	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the catalytic step does not require substantial structural flexibility or rearrangements	Homo sapiens	?	-	?

Subunits

Subunits	Comment	Organism
More	solution structures of the A-domain of ATP7A and ATP7B, solved by heteronuclear NMR spectroscopy, and dynamics of the A-domain of ATP7A, structure modeling, overview. The catalytically important TGE loop protrudes from the structure ready for interaction with the phosphorilated site in the ATP-binding domain	Homo sapiens

General Information

General Information	Comment	Organism
additional information	in humans, mutations in the ATP7A and ATP7B genes cause improper function of these copper(I)-ATPases, leading to severe inheritable diseases that involve dysfunctional copper homeostasis, named Menkes and Wilson diseases, respectively	Homo sapiens
physiological function	ATP7A and ATP7B are two human P1B-type ATPases that have a crucial role in maintaining copper(I) homeostasis	Homo sapiens

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Release 2023.1 (January 2023)